Resolution of the phosphoenolpyruvate: fructose phosphotransferase system of Escherichia coli into two components; enzyme IIfructose and fructose-induced HPr-like protein (FPr)
- 1 October 1980
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 58 (10) , 1144-1146
- https://doi.org/10.1139/o80-153
Abstract
A protein that substitutes for histidine-containing protein (HPr) in the phosphoenolpyruvate: fructose phosphotransferase system has been found in E. coli grown on fructose. The impure preparation of the fructose-induced HPr-like protein (FPr) appears to be an extrinsic membrane protein which differs from HPr on the basis of its appeparent MW (45,000 vs. 9600, respectively), its affinity for DEAE-cellulose and its ability to promote sugar phosphorylation which is specific for fructose, rather than for glucose.This publication has 7 references indexed in Scilit:
- Sugar transport. Properties of mutant bacteria defective in proteins of the phosphoenolpyruvate: sugar phosphotransferase system.Published by Elsevier ,2021
- Enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system of Escherichia coli. Purification to homogeneity and some propertiesCanadian Journal of Biochemistry, 1980
- Modified assay procedures for the phosphotransferase system in enteric bacteriaAnalytical Biochemistry, 1979
- Mycoplasma phosphoenolpyruvate-dependent sugar phosphotransferase system: glucose-negative mutant and regulation of intracellular cyclic AMPJournal of Bacteriology, 1978
- ?-Isopropylmalate synthase from Alcaligenes eutrophus H 16Archiv für Mikrobiologie, 1977
- 3-Deoxy-3-fluoro-D-glucose-resistant Salmonella typhimurium mutants defective in the phosphoenolpyruvate:glycose phosphotransferase systemJournal of Bacteriology, 1976
- Catabolism of d-fructose and d-ribose by Pseudomonas doudoroffiiArchiv für Mikrobiologie, 1975